Journal
JOURNAL OF GENERAL PHYSIOLOGY
Volume 150, Issue 11, Pages 1472-1483Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1085/jgp.201812153
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Funding
- National Institutes of Health [R01 GM120260, R21 GM126476]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM120260, R21GM126476] Funding Source: NIH RePORTER
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In 1918, the year the Journal of General Physiology was founded, there was little understanding of the structure of the cell membrane. It was evident that cells had invisible barriers separating the cytoplasm from the external solution. However, it would take decades before lipid bilayers were identified as the essential constituent of membranes. It would take even longer before it was accepted that there existed hydrophobic proteins that were embedded within the membrane and that these proteins were responsible for selective permeability in cells. With a combination of intuitive experiments and quantitative thinking, the last century of cell membrane research has led us to a molecular understanding of the structure of the membrane, as well as many of the proteins embedded within. Now, research is turning toward a physical understanding of the reactions of membrane proteins and lipids in this unique and incredibly complex solvent environment.
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